1JTD

Crystal structure of beta-lactamase inhibitor protein-II in complex with TEM-1 beta-lactamase

Summary for 1JTD

• Entry DOI: 10.2210/pdb1jtd/pdb
• Descriptor: TEM-1 beta-lactamase, beta-lactamase inhibitor protein II, CALCIUM ION, ... (4 entities in total)
• Functional Keywords: protein-protein complex, tem-1 beta-lactamase, beta-lactamase inhibitor protein-ii, blip-ii, hydrolase-inhibitor complex, hydrolase/inhibitor
• Biological source: Escherichia coli; More
• Total number of polymer chains: 2
• Total formula weight: 56527.41

Authors

Lim, D.C.,Park, H.U.,De Castro, L.,Kang, S.G.,Lee, H.S.,Jensen, S.,Lee, K.J.,Strynadka, N.C.J. (deposition date: 2001-08-20, release date: 2001-10-03, Last modification date: 2024-10-30)

Primary citation

Lim, D.,Park, H.U.,De Castro, L.,Kang, S.G.,Lee, H.S.,Jensen, S.,Lee, K.J.,Strynadka, N.C.
Crystal structure and kinetic analysis of beta-lactamase inhibitor protein-II in complex with TEM-1 beta-lactamase.
Nat.Struct.Biol., 8:848-852, 2001

PubMed Abstract: The structure of the 28 kDa beta-lactamase inhibitor protein-II (BLIP-II) in complex with the TEM-1 beta-lactamase has been determined to 2.3 A resolution. BLIP-II is a secreted protein produced by the soil bacterium Streptomyces exfoliatus SMF19 and is able to bind and inhibit TEM-1 with subnanomolar affinity. BLIP-II is a seven-bladed beta-propeller with a unique blade motif consisting of only three antiparallel beta-strands. The overall fold is highly similar to the core structure of the human regulator of chromosome condensation (RCC1). Although BLIP-II does not share the same fold with BLIP, the first beta-lactamase inhibitor protein for which structural data was available, a comparison of the two complexes reveals a number of similarities and provides further insights into key components of the TEM-1-BLIP and TEM-1-BLIP-II interfaces. Our preliminary results from gene knock-out studies and scanning electron microscopy also reveal a critical role of BLIP-II in sporulation.

PubMed: 11573088
DOI: 10.1038/nsb1001-848

Experimental method

X-RAY DIFFRACTION (2.3 Å)